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X-ray structures from the maltose-maltodextrin binding protein of the thermoacidophilic bacterium alicyclobacillus acidocaldarius
Analyse X-ray structures from the maltose-maltodextrin binding protein of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1URG
- Type
- protein
- Length
- 373 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding protein
- UniProt
- Q9RHZ6
- Ligands
- GLC
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding protein | protein | 373 | 46% helix, 19% strand | Q9RHZ6 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.64 | 0.77 | 40 | GLC |
| 2 | 179 | 0.49 | 0.77 | 30 | empty |
Compared structures
- 1URG · X-ray structures from the maltose-maltodextrin binding protein of the thermoacidophilic… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9RHZ6
- Elsewhere: RCSB PDB 1URG · PDBe 1URG · UniProt Q9RHZ6
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